A conserved ankyrin repeat-containing protein regulates conoid stability, motility and cell invasion in Toxoplasma gondii

Apicomplexan parasites are typified by an apical complex that contains a unique microtubule-organizing center (MTOC) that organizes the cytoskeleton. In apicomplexan parasites such as Toxoplasma gondii , the apical complex includes a spiral cap of tubulin-rich fibers called the conoid. Although desc...

Full description

Saved in:
Bibliographic Details
Published in:Nature communications 2017-12, Vol.8 (1), p.2236-2236, Article 2236
Main Authors: Long, Shaojun, Anthony, Bryan, Drewry, Lisa L., Sibley, L. David
Format: Article
Language:English
Subjects:
631/326/417/1716
631/80/128/1653
Ankyrin Repeat
Ankyrins
Apicomplexa - genetics
Apicomplexa - metabolism
Coils
Cytoskeleton
Cytoskeleton - metabolism
Fibers
Humanities and Social Sciences
Microtubule-Organizing Center - metabolism
Microtubule-Organizing Center - ultrastructure
Motility
Movement
multidisciplinary
Network analysis
Parasites
Proteins
Proteome - metabolism
Protozoa
Protozoan Proteins - genetics
Protozoan Proteins - metabolism
Science
Science (multidisciplinary)
Structural integrity
Structural proteins
Toxoplasma - genetics
Toxoplasma - metabolism
Toxoplasma - pathogenicity
Toxoplasma - ultrastructure
Toxoplasma gondii
Tubulin
Tubulin - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c606t-6d2e40fea68072fb34bc2d29f6670fd9feb9f3887759f44efa493f4d0758dfc23
cites cdi_FETCH-LOGICAL-c606t-6d2e40fea68072fb34bc2d29f6670fd9feb9f3887759f44efa493f4d0758dfc23
container_end_page 2236
container_issue 1
container_start_page 2236
container_title Nature communications
container_volume 8
creator Long, Shaojun
Anthony, Bryan
Drewry, Lisa L.
Sibley, L. David
description Apicomplexan parasites are typified by an apical complex that contains a unique microtubule-organizing center (MTOC) that organizes the cytoskeleton. In apicomplexan parasites such as Toxoplasma gondii , the apical complex includes a spiral cap of tubulin-rich fibers called the conoid. Although described ultrastructurally, the composition and functions of the conoid are largely unknown. Here, we localize 11 previously undescribed apical proteins in T . gondii and identify an essential component named conoid protein hub 1 (CPH1), which is conserved in apicomplexan parasites. CPH1 contains ankyrin repeats that are required for structural integrity of the conoid, parasite motility, and host cell invasion. Proximity labeling and protein interaction network analysis reveal that CPH1 functions as a hub linking key motor and structural proteins that contain intrinsically disordered regions and coiled coil domains. Our findings highlight the importance of essential protein hubs in controlling biological networks of MTOCs in early-branching protozoan parasites. Apicomplexan parasites such as Toxoplasma gondii possess a tubulin-rich structure called the conoid. Here, Long et al. identify a conoid protein that interacts with motor and structural proteins and is required for structural integrity of the conoid, parasite motility, and host cell invasion.
doi_str_mv 10.1038/s41467-017-02341-2
format article
fullrecord <record><control><sourceid>proquest_doaj_</sourceid><recordid>TN_cdi_doaj_primary_oai_doaj_org_article_33465d3f02bd4bd9a33944962a813a84</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_33465d3f02bd4bd9a33944962a813a84</doaj_id><sourcerecordid>1983426891</sourcerecordid><originalsourceid>FETCH-LOGICAL-c606t-6d2e40fea68072fb34bc2d29f6670fd9feb9f3887759f44efa493f4d0758dfc23</originalsourceid><addsrcrecordid>eNp1kk1r3DAQhk1paUKaP9BDEfTSQ93qy5J1KYTQj0Cgl_QsZEtytbUlV5KX7L-vvE7DplCB0KB559FoeKvqNYIfECTtx0QRZbyGqGxMKKrxs-ocwxIgjsnzk_isukxpB8siArWUvqzOsMBMcCzOq8MV6INPJu6NBsr_OkTnQTSzUbkuiaycd34AcwzZHDPDMqps0loVnAYpq86NLh_egynkY1QwGvRmHIHze5Vc8CUAd-E-zKNKkwJD8Nq5V9ULq8ZkLh_Oi-rHl89319_q2-9fb66vbuueQZZrprGh0BrFWsix7QjteqyxsIxxaLWwphOWtC3njbCUGquoIJZqyJtW2x6Ti-pm4-qgdnKOblLxIINy8ngR4iBVzK4fjSSEskYTC3GnaaeFIkRQKhhWLSKqpYX1aWPNSzcZ3RufoxqfQJ9mvPsph7CXDacQQV4A7x4AMfxeTMpycmmdlfImLEkiwYVgDWVr32__ke7CEn0ZVVG1hGLWClRUeFP1MaQUjX1sBkG5GkVuRpHFKPJoFLmi35x-47Hkry2KgGyCVFJ-MPHk7f9j_wD1Xcso</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1983426891</pqid></control><display><type>article</type><title>A conserved ankyrin repeat-containing protein regulates conoid stability, motility and cell invasion in Toxoplasma gondii</title><source>Open Access: PubMed Central</source><source>Publicly Available Content (ProQuest)</source><source>Nature Journals Online</source><source>Springer Nature - nature.com Journals - Fully Open Access</source><creator>Long, Shaojun ; Anthony, Bryan ; Drewry, Lisa L. ; Sibley, L. David</creator><creatorcontrib>Long, Shaojun ; Anthony, Bryan ; Drewry, Lisa L. ; Sibley, L. David</creatorcontrib><description>Apicomplexan parasites are typified by an apical complex that contains a unique microtubule-organizing center (MTOC) that organizes the cytoskeleton. In apicomplexan parasites such as Toxoplasma gondii , the apical complex includes a spiral cap of tubulin-rich fibers called the conoid. Although described ultrastructurally, the composition and functions of the conoid are largely unknown. Here, we localize 11 previously undescribed apical proteins in T . gondii and identify an essential component named conoid protein hub 1 (CPH1), which is conserved in apicomplexan parasites. CPH1 contains ankyrin repeats that are required for structural integrity of the conoid, parasite motility, and host cell invasion. Proximity labeling and protein interaction network analysis reveal that CPH1 functions as a hub linking key motor and structural proteins that contain intrinsically disordered regions and coiled coil domains. Our findings highlight the importance of essential protein hubs in controlling biological networks of MTOCs in early-branching protozoan parasites. Apicomplexan parasites such as Toxoplasma gondii possess a tubulin-rich structure called the conoid. Here, Long et al. identify a conoid protein that interacts with motor and structural proteins and is required for structural integrity of the conoid, parasite motility, and host cell invasion.</description><identifier>ISSN: 2041-1723</identifier><identifier>EISSN: 2041-1723</identifier><identifier>DOI: 10.1038/s41467-017-02341-2</identifier><identifier>PMID: 29269729</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/326/417/1716 ; 631/80/128/1653 ; Ankyrin Repeat ; Ankyrins ; Apicomplexa - genetics ; Apicomplexa - metabolism ; Coils ; Cytoskeleton ; Cytoskeleton - metabolism ; Fibers ; Humanities and Social Sciences ; Microtubule-Organizing Center - metabolism ; Microtubule-Organizing Center - ultrastructure ; Motility ; Movement ; multidisciplinary ; Network analysis ; Parasites ; Proteins ; Proteome - metabolism ; Protozoa ; Protozoan Proteins - genetics ; Protozoan Proteins - metabolism ; Science ; Science (multidisciplinary) ; Structural integrity ; Structural proteins ; Toxoplasma - genetics ; Toxoplasma - metabolism ; Toxoplasma - pathogenicity ; Toxoplasma - ultrastructure ; Toxoplasma gondii ; Tubulin ; Tubulin - metabolism</subject><ispartof>Nature communications, 2017-12, Vol.8 (1), p.2236-2236, Article 2236</ispartof><rights>The Author(s) 2017</rights><rights>2017. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c606t-6d2e40fea68072fb34bc2d29f6670fd9feb9f3887759f44efa493f4d0758dfc23</citedby><cites>FETCH-LOGICAL-c606t-6d2e40fea68072fb34bc2d29f6670fd9feb9f3887759f44efa493f4d0758dfc23</cites><orcidid>0000-0001-7110-0285</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1983426891/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1983426891?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25752,27923,27924,37011,37012,44589,53790,53792,74997</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29269729$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Long, Shaojun</creatorcontrib><creatorcontrib>Anthony, Bryan</creatorcontrib><creatorcontrib>Drewry, Lisa L.</creatorcontrib><creatorcontrib>Sibley, L. David</creatorcontrib><title>A conserved ankyrin repeat-containing protein regulates conoid stability, motility and cell invasion in Toxoplasma gondii</title><title>Nature communications</title><addtitle>Nat Commun</addtitle><addtitle>Nat Commun</addtitle><description>Apicomplexan parasites are typified by an apical complex that contains a unique microtubule-organizing center (MTOC) that organizes the cytoskeleton. In apicomplexan parasites such as Toxoplasma gondii , the apical complex includes a spiral cap of tubulin-rich fibers called the conoid. Although described ultrastructurally, the composition and functions of the conoid are largely unknown. Here, we localize 11 previously undescribed apical proteins in T . gondii and identify an essential component named conoid protein hub 1 (CPH1), which is conserved in apicomplexan parasites. CPH1 contains ankyrin repeats that are required for structural integrity of the conoid, parasite motility, and host cell invasion. Proximity labeling and protein interaction network analysis reveal that CPH1 functions as a hub linking key motor and structural proteins that contain intrinsically disordered regions and coiled coil domains. Our findings highlight the importance of essential protein hubs in controlling biological networks of MTOCs in early-branching protozoan parasites. Apicomplexan parasites such as Toxoplasma gondii possess a tubulin-rich structure called the conoid. Here, Long et al. identify a conoid protein that interacts with motor and structural proteins and is required for structural integrity of the conoid, parasite motility, and host cell invasion.</description><subject>631/326/417/1716</subject><subject>631/80/128/1653</subject><subject>Ankyrin Repeat</subject><subject>Ankyrins</subject><subject>Apicomplexa - genetics</subject><subject>Apicomplexa - metabolism</subject><subject>Coils</subject><subject>Cytoskeleton</subject><subject>Cytoskeleton - metabolism</subject><subject>Fibers</subject><subject>Humanities and Social Sciences</subject><subject>Microtubule-Organizing Center - metabolism</subject><subject>Microtubule-Organizing Center - ultrastructure</subject><subject>Motility</subject><subject>Movement</subject><subject>multidisciplinary</subject><subject>Network analysis</subject><subject>Parasites</subject><subject>Proteins</subject><subject>Proteome - metabolism</subject><subject>Protozoa</subject><subject>Protozoan Proteins - genetics</subject><subject>Protozoan Proteins - metabolism</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Structural integrity</subject><subject>Structural proteins</subject><subject>Toxoplasma - genetics</subject><subject>Toxoplasma - metabolism</subject><subject>Toxoplasma - pathogenicity</subject><subject>Toxoplasma - ultrastructure</subject><subject>Toxoplasma gondii</subject><subject>Tubulin</subject><subject>Tubulin - metabolism</subject><issn>2041-1723</issn><issn>2041-1723</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNp1kk1r3DAQhk1paUKaP9BDEfTSQ93qy5J1KYTQj0Cgl_QsZEtytbUlV5KX7L-vvE7DplCB0KB559FoeKvqNYIfECTtx0QRZbyGqGxMKKrxs-ocwxIgjsnzk_isukxpB8siArWUvqzOsMBMcCzOq8MV6INPJu6NBsr_OkTnQTSzUbkuiaycd34AcwzZHDPDMqps0loVnAYpq86NLh_egynkY1QwGvRmHIHze5Vc8CUAd-E-zKNKkwJD8Nq5V9ULq8ZkLh_Oi-rHl89319_q2-9fb66vbuueQZZrprGh0BrFWsix7QjteqyxsIxxaLWwphOWtC3njbCUGquoIJZqyJtW2x6Ti-pm4-qgdnKOblLxIINy8ngR4iBVzK4fjSSEskYTC3GnaaeFIkRQKhhWLSKqpYX1aWPNSzcZ3RufoxqfQJ9mvPsph7CXDacQQV4A7x4AMfxeTMpycmmdlfImLEkiwYVgDWVr32__ke7CEn0ZVVG1hGLWClRUeFP1MaQUjX1sBkG5GkVuRpHFKPJoFLmi35x-47Hkry2KgGyCVFJ-MPHk7f9j_wD1Xcso</recordid><startdate>20171221</startdate><enddate>20171221</enddate><creator>Long, Shaojun</creator><creator>Anthony, Bryan</creator><creator>Drewry, Lisa L.</creator><creator>Sibley, L. David</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><general>Nature Portfolio</general><scope>C6C</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7T7</scope><scope>7TM</scope><scope>7TO</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0001-7110-0285</orcidid></search><sort><creationdate>20171221</creationdate><title>A conserved ankyrin repeat-containing protein regulates conoid stability, motility and cell invasion in Toxoplasma gondii</title><author>Long, Shaojun ; Anthony, Bryan ; Drewry, Lisa L. ; Sibley, L. David</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c606t-6d2e40fea68072fb34bc2d29f6670fd9feb9f3887759f44efa493f4d0758dfc23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>631/326/417/1716</topic><topic>631/80/128/1653</topic><topic>Ankyrin Repeat</topic><topic>Ankyrins</topic><topic>Apicomplexa - genetics</topic><topic>Apicomplexa - metabolism</topic><topic>Coils</topic><topic>Cytoskeleton</topic><topic>Cytoskeleton - metabolism</topic><topic>Fibers</topic><topic>Humanities and Social Sciences</topic><topic>Microtubule-Organizing Center - metabolism</topic><topic>Microtubule-Organizing Center - ultrastructure</topic><topic>Motility</topic><topic>Movement</topic><topic>multidisciplinary</topic><topic>Network analysis</topic><topic>Parasites</topic><topic>Proteins</topic><topic>Proteome - metabolism</topic><topic>Protozoa</topic><topic>Protozoan Proteins - genetics</topic><topic>Protozoan Proteins - metabolism</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Structural integrity</topic><topic>Structural proteins</topic><topic>Toxoplasma - genetics</topic><topic>Toxoplasma - metabolism</topic><topic>Toxoplasma - pathogenicity</topic><topic>Toxoplasma - ultrastructure</topic><topic>Toxoplasma gondii</topic><topic>Tubulin</topic><topic>Tubulin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Long, Shaojun</creatorcontrib><creatorcontrib>Anthony, Bryan</creatorcontrib><creatorcontrib>Drewry, Lisa L.</creatorcontrib><creatorcontrib>Sibley, L. David</creatorcontrib><collection>SpringerOpen</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>Advanced Technologies &amp; Aerospace Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Biological Science Database</collection><collection>Advanced Technologies &amp; Aerospace Database</collection><collection>ProQuest Advanced Technologies &amp; Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Publicly Available Content (ProQuest)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Open Access: DOAJ - Directory of Open Access Journals</collection><jtitle>Nature communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Long, Shaojun</au><au>Anthony, Bryan</au><au>Drewry, Lisa L.</au><au>Sibley, L. David</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A conserved ankyrin repeat-containing protein regulates conoid stability, motility and cell invasion in Toxoplasma gondii</atitle><jtitle>Nature communications</jtitle><stitle>Nat Commun</stitle><addtitle>Nat Commun</addtitle><date>2017-12-21</date><risdate>2017</risdate><volume>8</volume><issue>1</issue><spage>2236</spage><epage>2236</epage><pages>2236-2236</pages><artnum>2236</artnum><issn>2041-1723</issn><eissn>2041-1723</eissn><abstract>Apicomplexan parasites are typified by an apical complex that contains a unique microtubule-organizing center (MTOC) that organizes the cytoskeleton. In apicomplexan parasites such as Toxoplasma gondii , the apical complex includes a spiral cap of tubulin-rich fibers called the conoid. Although described ultrastructurally, the composition and functions of the conoid are largely unknown. Here, we localize 11 previously undescribed apical proteins in T . gondii and identify an essential component named conoid protein hub 1 (CPH1), which is conserved in apicomplexan parasites. CPH1 contains ankyrin repeats that are required for structural integrity of the conoid, parasite motility, and host cell invasion. Proximity labeling and protein interaction network analysis reveal that CPH1 functions as a hub linking key motor and structural proteins that contain intrinsically disordered regions and coiled coil domains. Our findings highlight the importance of essential protein hubs in controlling biological networks of MTOCs in early-branching protozoan parasites. Apicomplexan parasites such as Toxoplasma gondii possess a tubulin-rich structure called the conoid. Here, Long et al. identify a conoid protein that interacts with motor and structural proteins and is required for structural integrity of the conoid, parasite motility, and host cell invasion.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>29269729</pmid><doi>10.1038/s41467-017-02341-2</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0001-7110-0285</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 2041-1723
ispartof Nature communications, 2017-12, Vol.8 (1), p.2236-2236, Article 2236
issn 2041-1723
2041-1723
language eng
recordid cdi_doaj_primary_oai_doaj_org_article_33465d3f02bd4bd9a33944962a813a84
source Open Access: PubMed Central; Publicly Available Content (ProQuest); Nature Journals Online; Springer Nature - nature.com Journals - Fully Open Access
subjects 631/326/417/1716
631/80/128/1653
Ankyrin Repeat
Ankyrins
Apicomplexa - genetics
Apicomplexa - metabolism
Coils
Cytoskeleton
Cytoskeleton - metabolism
Fibers
Humanities and Social Sciences
Microtubule-Organizing Center - metabolism
Microtubule-Organizing Center - ultrastructure
Motility
Movement
multidisciplinary
Network analysis
Parasites
Proteins
Proteome - metabolism
Protozoa
Protozoan Proteins - genetics
Protozoan Proteins - metabolism
Science
Science (multidisciplinary)
Structural integrity
Structural proteins
Toxoplasma - genetics
Toxoplasma - metabolism
Toxoplasma - pathogenicity
Toxoplasma - ultrastructure
Toxoplasma gondii
Tubulin
Tubulin - metabolism
title A conserved ankyrin repeat-containing protein regulates conoid stability, motility and cell invasion in Toxoplasma gondii
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T12%3A52%3A15IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_doaj_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20conserved%20ankyrin%20repeat-containing%20protein%20regulates%20conoid%20stability,%20motility%20and%20cell%20invasion%20in%20Toxoplasma%20gondii&rft.jtitle=Nature%20communications&rft.au=Long,%20Shaojun&rft.date=2017-12-21&rft.volume=8&rft.issue=1&rft.spage=2236&rft.epage=2236&rft.pages=2236-2236&rft.artnum=2236&rft.issn=2041-1723&rft.eissn=2041-1723&rft_id=info:doi/10.1038/s41467-017-02341-2&rft_dat=%3Cproquest_doaj_%3E1983426891%3C/proquest_doaj_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c606t-6d2e40fea68072fb34bc2d29f6670fd9feb9f3887759f44efa493f4d0758dfc23%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1983426891&rft_id=info:pmid/29269729&rfr_iscdi=true